Source:http://linkedlifedata.com/resource/pubmed/id/17141727
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2007-2-27
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pubmed:abstractText |
Alpha1-antitrypsin is well known for its ability to inhibit human neutrophil elastase. Pretreatment of alpha1-antitrypsin with hypohalous acids HOCl and HOBr as well as with the myeloperoxidase-hydrogen peroxide-chloride (or bromide) system inactivated this proteinase. The flavonols rutin, quercetin, myricetin, and kaempferol inhibited the inactivation of alpha1-antitrypsin by HOCl and HOBr with rutin having the most pronounced effect. In contrast, these flavonols did not remove the proteinase inactivation by the myeloperoxidase-hydrogen peroxide-halide system. Taurine did not protect against the inactivation of alpha1-antitrypsin by HOCl, HOBr, or the myeloperoxidase-hydrogen peroxide-halide system, while methionine was efficient in all systems. A close association between myeloperoxidase and alpha1-antitrypsin was revealed by native gel electrophoresis and in-gel peroxidase staining. In addition, alpha1-antitrypsin binds to the myeloperoxidase components transferred after SDS-PAGE on a blotting membrane. With this complex formation, myeloperoxidase overcomes the natural antioxidative protective system of plasma and prevents the inactivation of alpha1-antitrypsin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bromates,
http://linkedlifedata.com/resource/pubmed/chemical/Flavonols,
http://linkedlifedata.com/resource/pubmed/chemical/Halogens,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Hypochlorous Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/alpha 1-Antitrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/hypobromous acid
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
459
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
137-42
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pubmed:meshHeading |
pubmed-meshheading:17141727-Bromates,
pubmed-meshheading:17141727-Enzyme Activation,
pubmed-meshheading:17141727-Flavonols,
pubmed-meshheading:17141727-Halogens,
pubmed-meshheading:17141727-Hydrogen Peroxide,
pubmed-meshheading:17141727-Hypochlorous Acid,
pubmed-meshheading:17141727-Peroxidase,
pubmed-meshheading:17141727-alpha 1-Antitrypsin
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pubmed:year |
2007
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pubmed:articleTitle |
Differential effects of flavonols on inactivation of alpha1-antitrypsin induced by hypohalous acids and the myeloperoxidase-hydrogen peroxide-halide system.
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pubmed:affiliation |
Laboratory of Applied Biochemistry, Department of Biology, Faculty of Sciences, University of Ferhat ABBAS, 19000 Setif, Algeria.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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